Q5J6J3 (DPP4_TRIRU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidyl peptidase 4
EC=3.4.14.5

Alternative name(s):
Dipeptidyl peptidase IV
Short name=DPP IV
Short name=DppIV

Gene names

Name:

DPP4

Organism

Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)

Taxonomic identifier

5551 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Onygenales › Arthrodermataceae › mitosporic Arthrodermataceae › Trichophyton

Protein attributes

Sequence length	775 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Contributes to pathogenicity. Ref.1
Catalytic activity	Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
Subcellular location	Secreted Ref.1.
Sequence similarities	Belongs to the peptidase S9B family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0-9.0. Ref.1

Ontologies

Keywords
Biological process	Virulence
Cellular component	Secreted
Domain	Signal
Molecular function	Aminopeptidase Hydrolase Protease Serine protease
PTM	Glycoprotein
Gene Ontology (GO)
Biological_process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15	Potential
	Chain	16 – 775	760	Dipeptidyl peptidase 4		PRO_0000384089
Sites
	Active site	613	1	Charge relay system By similarity
	Active site	690	1	Charge relay system By similarity
	Active site	725	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	81	1	N-linked (GlcNAc...) Potential
	Glycosylation	111	1	N-linked (GlcNAc...) Potential
	Glycosylation	154	1	N-linked (GlcNAc...) Potential
	Glycosylation	219	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5J6J3 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 157774F128C6BFDB	FASTA	775	88,021
	10 20 30 40 50 60 MKLLSLLMLA GIAQAIVPPR EPRSPTGGGN KLLTYKECVP RATISPRSTS LAWINSEEDG 70 80 90 100 110 120 RYISQSDDGA LILQNIVTNT NKTLVAADKV PKGYYDYWFK PDLSAVLWAT NYTKQYRHSY 130 140 150 160 170 180 FANYFILDIK KGSLTPLAQD QAGDIQYAQW SPMNNSIAYV RXNDLYIWNN GKTKRITENG 190 200 210 220 230 240 GPDIFNGVPD WVYEEEIFGD RFALWFSPDG EYLAYLRFNE TGVPTYTIPY YKNKQKIAPA 250 260 270 280 290 300 YPRELEIRYP KVSAKNPTVQ FHLLNIASSQ ETTIPVTAFP ENDLVIGEVA WLSSGHDSVA 310 320 330 340 350 360 YRAFNRVQDR EKIVSVKVES KESKVIRERD GTDGWIDNLL SMSYIGNVNG KEYYVDISDA 370 380 390 400 410 420 SGWAHIYLYP VDGGKEIALT KGEWEVVAIL KVDTKKKLIY FTSTKYHSTT RHVYSVSYDT 430 440 450 460 470 480 KVMTPLVNDK EAAYYTASFS AKGGYYILSY QGPNVPYQEL YSTKDSKKPL KTITSNDALL 490 500 510 520 530 540 EKLKEYKLPK VSFFEIKLPS GETLNVKQRL PPNFNPHKKY PVLFTPYGGP GAQEVSQAWN 550 560 570 580 590 600 SLDFKSYITS DPELEYVTWT VDNRGTGYKG RKFRSAVAKR LGFLEAQDQV FAAKEVLKNR 610 620 630 640 650 660 WADKDHIGIW GXSYGGFLTA KTLETDSGVF TFGISTAPVS DFRLYDSMYT ERYMKTVELN 670 680 690 700 710 720 ADGYSETAVH KVDGFKNLKG HYLIQHGTGD DNVHFQNAAV LSNTLMNGGV TADKLTTQWF 730 740 750 760 770 TDSDHGIRYD MDSTYQYKQL SKMVYDQKQR RPESPPMHQW SKRVLAALFG ERAEE

References

[1]

"Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum." Monod M., Lechenne B., Jousson O., Grand D., Zaugg C., Stoecklin R., Grouzmann E. Microbiology 151:145-155(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY497021 Genomic DNA. Translation: AAS76665.1.
3D structure databases
HSSP	HSSP built from PDB template 1PFQ based on UniProtKB P27487.
ProteinModelPortal	Q5J6J3.
ModBase	Search...
Protein family/group databases
MEROPS	S09.008.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002471. Pept_S9_AS. IPR001375. Peptidase_S9. IPR002469. Peptidase_S9B. [Graphical view]
Pfam	PF00930. DPPIV_N. 1 hit. PF00326. Peptidase_S9. 1 hit. [Graphical view]
PROSITE	PS00131. CARBOXYPEPT_SER_SER. 1 hit. PS00708. PRO_ENDOPEP_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPP4_TRIRU

Accession

Primary (citable) accession number: Q5J6J3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	February 15, 2005
Last modified:	June 13, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program